ID   BLAC_STRFR              Reviewed;         306 AA.
AC   P35392; P72435;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Beta-lactamase;
DE            EC=3.5.2.6;
DE   AltName: Full=Penicillinase;
DE   Flags: Precursor;
GN   Name=blaF;
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB
RC   8233 / NRRL B-1195 / VKM Ac-150;
RX   PubMed=2391494; DOI=10.1099/00221287-136-3-589;
RA   Forsman M., Haeggstroem B., Lindgren L., Jaurin B.;
RT   "Molecular analysis of beta-lactamases from four species of Streptomyces:
RT   comparison of amino acid sequences with those of other beta-lactamases.";
RL   J. Gen. Microbiol. 136:589-598(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX   PubMed=1385267; DOI=10.1016/0378-1119(92)90165-l;
RA   Forsman M., Granstroem M.;
RT   "Mutagenic analysis of the promoter of the Streptomyces fradiae beta-
RT   lactamase-encoding gene.";
RL   Gene 121:87-94(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; M34179; AAA26709.1; -; Genomic_DNA.
DR   EMBL; M94255; AAC41397.1; -; Genomic_DNA.
DR   PIR; B45822; B45822.
DR   AlphaFoldDB; P35392; -.
DR   SMR; P35392; -.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..34
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           35..306
FT                   /note="Beta-lactamase"
FT                   /id="PRO_0000017018"
FT   ACT_SITE        82
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  32931 MW;  8FAEF14220812A17 CRC64;
     MDRTTARPNR RAVLATGVGA ALAATAAAAG PAHAAPGRGA RVEGRLRALE RTHDARLGAF
     AYDTGTGRTV AYRADERFPI ASMFKTIAVA AVLRDLDRDG EVLARRVHYT ADYVKRSGYS
     PVTGLPENVA NGMTVAELCE ATLTRSDNTA ANLLLRDLGG PTAVTRFCRS VGDHVTRLDR
     WEPELNSAEP GRVTDTTSPR AIGRTYGRLI LGDLLAAHDR ERLTRWMLDN RTSDERFRKG
     LPADWLLADK TGGGDYGTNN DAGVAWPPGR PPVVLAVQTT RFTPDAEADN VLVAEAARLL
     AEAMTD